HSP90 Resource Guide HSP90

Heat Shock Protein 90 HSP90 information database. A resource for all HSP90 structure, isoform, function, disease relevance, and inhibitor information.

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LINKS TO WEBSITE

HSP27 Scientific Resource Guide HSP27

And is the human homologue of murine Hsp25. Throughout this website, Hsp27 and HspB1 will be used interchangeably. Hsp27 is ubiquitously expressed and has been implicated in various biological functions. In contrast to large Hsps, Hsp27 acts through ATP-independent mechanisms, and. Activation of the heat shock-responsive element on the.

HSP40 Introduction HSP40

Relevant database IDs for Human.

HSP60 Introduction HSP60

HSP60 chaperones can be found not only in the cytosol, chloroplasts, hydrogenosomes and mitochondria. But also on the cell surface and in the extracellular milieu.

HSP70 Scientific Resource Guide

In many cases HSP70s can function redundantly. All of the cellular activities of HSP70s depend on their ATP-regulated ability to interact with exposed hydrophobic surfaces of proteins. Herein, focus is given on the regulation, function and disease relevance of the molecular HSP70 chaperones as well as their impact as therapeutic drug targets. Ribbon and tube representation of the tertiary Hsp70-1 structure in the presence of ADP.

Home - Hsp90

Next Hsp90 meeting will take place in Leysin, Switzerland. October 17 to 21, 2018. At one of the first Hsp90 meetings, in Gwatt in 2004, the idea came up that it would be useful for the community to have a dedicated and not-for-profit web site to serve as a focal point. The domain name was therefore registered by Didier Picard who is a basic research scientist working at an academic institution.

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HSP90 Resource Guide HSP90

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Heat Shock Protein 90 HSP90 information database. A resource for all HSP90 structure, isoform, function, disease relevance, and inhibitor information.

PARSED CONTENT

The website states the following, "HSP90 proteins define a widespread family of molecular chaperones found in bacteria and all eukaryotes playing a fundamental role in protein homoeostasis and viability." I analyzed that the web page also said " HSP90s primarily exist as homodimers whose activity is regulated by ATP." They also stated " HSP90 chaperones can be found not only in the cytosol, ER, chloroplasts, mitochondria, and the nucleus. But also in the extracellular milieu where they act as potent stimulators of immune responses."

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